ID A0A151GMP8_9HYPO Unreviewed; 494 AA.
AC A0A151GMP8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=tryptophan--tRNA ligase {ECO:0000256|ARBA:ARBA00013161};
DE EC=6.1.1.2 {ECO:0000256|ARBA:ARBA00013161};
DE AltName: Full=Tryptophanyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030268};
GN ORFNames=DCS_05314 {ECO:0000313|EMBL:KYK58301.1};
OS Drechmeria coniospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Drechmeria.
OX NCBI_TaxID=98403 {ECO:0000313|EMBL:KYK58301.1, ECO:0000313|Proteomes:UP000076580};
RN [1] {ECO:0000313|EMBL:KYK58301.1, ECO:0000313|Proteomes:UP000076580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 6962 {ECO:0000313|EMBL:KYK58301.1,
RC ECO:0000313|Proteomes:UP000076580};
RX PubMed=26975455; DOI=10.1038/srep23122;
RA Zhang L., Zhou Z., Guo Q., Fokkens L., Miskei M., Pocsi I., Zhang W.,
RA Chen M., Wang L., Sun Y., Donzelli B.G., Gibson D.M., Nelson D.R.,
RA Luo J.G., Rep M., Liu H., Yang S., Wang J., Krasnoff S.B., Xu Y.,
RA Molnar I., Lin M.;
RT "Insights into Adaptations to a Near-Obligate Nematode Endoparasitic
RT Lifestyle from the Finished Genome of Drechmeria coniospora.";
RL Sci. Rep. 6:23122-23122(2016).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363036}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYK58301.1}.
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DR EMBL; LAYC01000002; KYK58301.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151GMP8; -.
DR STRING; 98403.A0A151GMP8; -.
DR InParanoid; A0A151GMP8; -.
DR OrthoDB; 540846at2759; -.
DR Proteomes; UP000076580; Chromosome 02.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00806; TrpRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR002306; Trp-tRNA-ligase.
DR NCBIfam; TIGR00233; trpS; 1.
DR PANTHER; PTHR10055:SF1; TRYPTOPHAN--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR10055; TRYPTOPHANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01039; TRNASYNTHTRP.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363036};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363036};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363036};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363036};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363036};
KW Reference proteome {ECO:0000313|Proteomes:UP000076580}.
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 460..487
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 494 AA; 54498 MW; 647CBB3818C3DBDB CRC64;
MASAPSQSAE PPSTVGQDGT APPASSTKQD INPWSVSGEV GEDGKVKAID YRKLVQEFGT
NLIDDALLER FERVTGHKPH RFMRRQIVFS HRDLSVILDR YEKNEPFYLY TGRGPSSDSM
HIGHTQVFDF VKWLQDVLDA PLIIMLTDDE KYLFSEKRTV EEVMGYTRTN VMDIIAVGFD
AEKTFIFSDF DFVGGAFYKN IVRFAKRVTY NTVRAIFGFD GSANIGKVHF ASIQGATAFA
SSFPHIFGPD ESKTASIPCL IPCAIDQDPY FRLTRDCAAG LHLAKPSLIH MRFLDALQGP
GSKMSASDDT SAIFLNDTAK QIKNKINKHA FSGGRETVEE HRELGGNADV DVSYQYLQFF
LEDDEELKRI KEDYNSGKLL TGELKAMCIE HLQKYVSGFQ ERRSKVTDAV VDEFMTARPL
KWNGNPKVPR ADLVVPVVAA GDADADGAAT AAGADGKMSK SQMKKLLKEQ QIAAKKAEKD
KAKAATKAAS SGGA
//
